[Synthesis and properties of carrier-bound enzymes. XI. Fixation of trypsin to various cellulose derivatives. Comparison of the kinetic properties of the trypsin-cellulose complexes]. / Synthese und Eigenschaften trägerfixierter Enzyme. XI. Fixierung von Trypsin an unterschliedliche Zekllulosederivate. Vergleich der kinetischen Eigenschaften der Trypsin-Zellulose-Komplexe.

Trypsin was covalently bound to carboxymethyl cellulose (CMC) azide and dialdehyde cellulose (DAC). Thereby the maximum protein binding capacity of CMC (420 mg/g) is 28 times that of DAC (15 mg/g). The high protein binding capacity of CMC is explained by a change in structure, i. e. by surface increase of the original cellulose powder due to chemical modification. By activation with sodium bisulfite solution we achieved an increase in protein binding capacity of DAC to values similar to those of CMC. The value of Vmax for all trypsin-DAC-complexes is about 38% of that of the free enzyme. With increasing protein content (from 1 to 12 mg/g) Km rises continuously from 0,14 to 0.36 mM. An analogous kinetic behaviour was found for trypsin-CMC-complexes only up to a protein content of 100 mg/g. Offering larger quantities of trypsin the enzyme is immobilized in an active form, so that all trypsin-CMC-complexes from 100 mg/g upwards have the same specific activity and the same Km; on the other hand the value of Vmax for the immobilized trypsin decreases to 17% of that for the free enzyme.

[Synthesis and properties of carrier-fixed enzymes. VII. Linking of glucoamylase to dialdehyde cellulose, carboxymethylcellulose hydrazide and carboxymethylcellulose azide]. / Synthese und Eigenschaften trägerfixierten Enzyme. VII. Fixierung von Glukoamylase an Dialdehydzellulose. Karboxymethylzellulosehydrazid und Karboxymethylzelluloseazid.

Glucoamylase (alpha-1,4-glucan glucohydrolase, EC 3.2.1.3) has been covalently linked to dialdehyde cellulose resulting in an immobilized enzyme containing 0.98% protein and an activity of 4.5 mg of the native enzyme per g of matrix, i.e. 46% relative activity. The complex lost its activity in continuous and batch hydrolysis of starch at 55 degrees C down to a limit of 18% of its original value. In contrast, the activity of the complex did not change when working at a temperature of 25 degrees C. Glucoamylase-carboxymethylcellulose complexes synthesized via carboxymethylcellulose hydrazide and azide, in contrast to MAEDA und SUZUKI [1], showed only an activity of 1 mg of the native enzyme per g of matrix. We did not succeed in coupling periodate-oxidized glucoamylase to carboxymethylcellulose hydrazide because the enzyme used lost nearly all of its activity already during periodate oxidation.

[Late results in hemialloarthroplasty of the hip (author's transl)]. / Spätergebnisse der Hemialloarthroplastik des Hüftgelenkes

This paper presents a study of long-term results of femoral head replacement. 104 patients with Moore prosthesis could be followed up for an average of 9 1/2 years. In cases of fractures and complications of trauma the results were excellent and good in 65%. Practically 100% poor results could be shown in patients with osteoarthritis